• Food Science of Animal Resources
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• v.35 no.5
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• pp.577-584
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• 2015

This study was conducted to evaluate the effect of pre-rigor salting level (0-4% NaCl concentration) on physicochemical and textural properties of pre-rigor chicken breast muscles. The pre-rigor chicken breast muscles were de-boned 10 min post-mortem and salted within 25 min post-mortem. An increase in pre-rigor salting level led to the formation of high ultimate pH of chicken breast muscles at post-mortem 24 h. The addition of minimum of 2% NaCl significantly improved water holding capacity, cooking loss, protein solubility, and hardness when compared to the non-salting chicken breast muscle (p<0.05). On the other hand, the increase in pre-rigor salting level caused the inhibition of myofibrillar protein degradation and the acceleration of lipid oxidation. However, the difference in NaCl concentration between 3% and 4% had no great differences in the results of physicochemical and textural properties due to pre-rigor salting effects (p>0.05). Therefore, our study certified the pre-rigor salting effect of chicken breast muscle salted with 2% NaCl when compared to post-rigor muscle salted with equal NaCl concentration, and suggests that the 2% NaCl concentration is minimally required to ensure the definite pre-rigor salting effect on chicken breast muscle.

• Digital Contents
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• no.12 s.127
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• pp.160-165
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• 2003

• Applied Biological Chemistry
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• v.14 no.2
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• pp.165-169
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• 1971

From both breast and leg muscle of 12 week-old broiler chicken held for aging in slushed ice and dry chilling at $33-35^{\circ}F$., myosin, actomyosin and other nitrogenous fractions were extracted with KCl-phosphate buffer for various periods from 1 hr. to 25 hr. post-mortem. The changes in extractable nitrogen occurred mainly as a result of decrease in extractability of myosin and to some extent, increase in extractability of actomyosin. Changes in stroma, sarcoplasmic and NPN fractions were small. Myosin extractability decreased rapidly during the first 3 hr. post-mortem and then reduced Continuously in both leg muscle and breast muscle during wet chilling. The decrease of myosin extractability in leg muscle was much more than that in breast muscle, and then the extractability increased after 17 hr. post-mortem in dry chilling. Actomyosin was extracted at low consistent level in wet chilling, while it increased considerably after 17 hr. post-mortem in dry chilling. The tendency was similar in both breast and leg muscle.

• Food Science of Animal Resources
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• v.40 no.3
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• pp.415-425
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• 2020

It is believed that two main proteolytic systems are involved in the tenderization of meat: the cathepsins and the calpains. Many researchers consider the calpain system to be the major contributor to meat tenderness during post-mortem storage. However, the role and activity of cathepsins during post-mortem storage or low temperature meat processing is unclear, particularly for the tough meat cuts like brisket. Thus, the study was designed to investigate the effects of cold (refrigerated and frozen) storage and sous vide processing on the activities of cathepsin B, H, and L in beef brisket. There were no significant changes in pH and cathepsin H activity throughout the 18 d of storage at both temperatures. However, an increase in cathepsin B activity was observed during the first 4 d at both storage temperatures, but subsequently the activity remained unchanged. Cathepsins B and L were found to be more heat stable at sous vide temperatures (50℃ for 24 h, 55℃ for 5 h and at 60℃ and 70℃ for 1 h) compared to cathepsin H. Cathepsin B+L activity was found to increase after sous vide cooking at 50℃ for 1 h but decreased to about 47% relative to the uncooked control after 24 h of cooking. These results suggest that cathepsins B and L may contribute to the improved meat tenderness usually seen in sous vide cooked brisket meat.

• Journal of Sasang Constitutional Medicine
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• v.18 no.2
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• pp.83-95
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• 2006

1. Objectives and Methods The purpose of this study was to objectify the diagnosis of Sasang constitution. It analyzed the adult male and female voices into 23factors using PSSC-2004. The study was conducted by subjects inputting 2.5-3 sec of [a] in 586 men and women's voices to PSSC-2004. The statistical analyses are applied to three groups: total group, male group, female group. The group with a total of 586 was composed of 155 Soyangin, 230 Taeumin and 201 Soeumin. The male group was composed with 61 Soyangin, 127 Taeumin and 87 Soeumin. The female group was composed with 94 Soyangin, 103 Taeumin and 114 Soeumin. Taeyangin were excluded for a more accurate statistical analysis. 2. Results (I) In total group, Taeumin's peak sum was significantly high compared with the others(P=0.021). It was significant for distinction between Taeumin and Soyangin at the result of post mortem. (2) In total group, the Soyangin's rank6, rank7 and rank8 were significantly high compared with the others (P=0.050)(0.043)(0.034). (3) In total group, the Soyangin's rank9 was significantly high compared with the others(P=0.025). It was significant for distinction between Taeumin and Soyangin at the result of post mortem. (4) In male group, the Soyangin's code3 was significantly high compared with the others(P=0.050). (5) In male group, the Soyangin's code1 was significantly low compared with the others(P=0.004). It was significant for distinction between Taeumin and Soyangin at the result of post mortem. (6) In male group, the Soyangin's rank1, rank2, rank3 and rank4 were significantly high compared with the others(P=0.017)(0.008) (0.005)(0.002). They were significant for distinction between Taeumin and Soyangin at the result of post mortem. (7) In female group, the Taeumin's code1 was significantly low compared with the others(P=0.016). It was significant for distinction between Taeumin and Soeumin at the result of post mortem. 3. Conclusion From above result, there is the possibility of efficiency standard gide for constitutional diagnosis by analyzation of the voices.

• Korean Journal of Food Science and Technology
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• v.9 no.4
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• pp.295-305
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• 1977

The procedures for the Preparation of regulatory proteins of myofibrill were developed and postmortem changes in the regulatory proteins of myofibrill were investigated. Both the physiological property and molecular shape of ${\alpha}-actinin$ from pre-rigor muscle did not differ from those of ${\alpha}-actinin$ from post-rigor muscle. On the other hand, although tropomyosin of myofibril changed negligibly during the post-mortem storage of muscle, troponin of myofibril changed remarkably.

• Animal Bioscience
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• v.34 no.11
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• pp.1849-1858
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• 2021

Objective: Tenderness is a very complex feature, and the process of its formation is very complicated and not fully understood. Its diversification is one of the most important problems of beef production, as a result beef aging is widely used to improve tenderness as it is believed to provide a homogeneous product to consumers. While few studies have evaluated the muscle structure properties in relation to tenderness from early post-mortem, there little to no information available on how the muscle nanostructure of beef carcasses changes during post-mortem ageing to determine the appropriate aging time for acceptable tenderness. Methods: Muscle nanostructure (myofibril diameter [MYD], myofibril spacing [MYS], muscle fibre diameter [MFD], muscle fibre spacing [MFS], and sarcomere length [SL]), meat tenderness and cooking loss [CL]) were measured on 20 A2 longissimus muscles of Bonsmara, Beefmaster, Hereford, and Simbra at 45_mins, 1, 3, and 7 days post-slaughter. Muscle nanostructure was measured using a scanning electron microscope, while tenderness was measured using Warner Bratzler shear force. Results: At 45 minutes post-slaughter, breed affected MYD and MYS only, while at 24_hrs it also affected MFD and MFS. On day 3 breed effected MFS and SL, while on day 7 breed effected tenderness only. As the muscles matured, both MYD and MYS decreased while CL increased, and the muscles became tender. There was no uniformity on muscle texture features (surface structure, fibre separation, muscle contraction, and relaxation) throughout the ageing period. Conclusion: Meat tenderness can be directly linked to breed related myofibril structure changes during aging in particular the MYD, spacing between myofibrils and their interaction; while the MFD, spacing between muscle fibres, SL, and CL explain the non-uniformity in beef tenderness.

• Proceedings of KOSOMES biannual meeting
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• 2018.06a
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• pp.10-10
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• 2018

• Korean journal of communication and information
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• v.68
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• pp.65-86
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• 2014

Photography is frequently associated with the death because it seems to remind us of our own mortality by representing the dead people. The indexical character of photography reinforces this association. Photography is used in many ceremonial activities and medias to represent death. Five types of death photography can be differentiated: funeral portrait, post-mortem photography, conflict and disaster photography, death penalty photography, anatomic and forensic photography. These death photographies serve for four individual and social purposes: mourning and remembrance, resistance and struggle, rule and domination, disclosure and accusation.

• Food Science of Animal Resources
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• v.18 no.4
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• pp.292-300
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• 1998

This study was undertaken to determine the influence in the Z-disk domain of titin on the tenderization of meat by the structure change of myofibrillar Z-disks during post-mortem aging. After weakening the structure of Z-disks, the Z-disk region was splitted. As the results, myofibrils were fragmented by mechanical strength. Using indirect immunofluorescence microscopy, we show that the Z-disk domain of titin was disappeared from myofibrils in this period. There phenomenon were also shown by treating myofibrils with a solution containing 0.1mM $Ca^{2+}$. We conclude that change in Z-disk domain of titin is directly effected on the tenderization of meat during post-mortem aging and these change is due to manily calcium ions.